CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014757
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit epsilon 
Protein Synonyms/Alias
 TCP-1-epsilon; CCT-epsilon 
Gene Name
 Cct5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
223GGRLEDTKLIKGVIVacetylation[1]
226LEDTKLIKGVIVDKDacetylation[1]
232IKGVIVDKDFSHPQMacetylation[1]
284LQKYEKEKFEEMIAQacetylation[1]
368EISFGTTKDKMLVIEacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 26 26 Phosphoserine (By similarity).  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 541 AA 
Protein Sequence
MASVGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM 60
MVDKDGDVTV TNDGATILSM MDVDHQIAKL MVELSKSQDD EIGDGTTGVV VLAGALLEEA 120
EQLLDRGIHP IRIADGYEQA ARIAIQHLDK ISDNVLVDIN NPEPLIQTAK TTLGSKVVNS 180
CHRQMAEIAV NAVLTVADME RRDVDFELIK VEGKVGGRLE DTKLIKGVIV DKDFSHPQMP 240
KEVLNAKIAI LTCPFEPPKP KTKHKLDVTS VEDYKALQKY EKEKFEEMIA QIKETGANLA 300
ICQWGFDDEA NHLLLQNGLP AVRWVGGPEI ELIAIATGGR IVPRFSELTS EKLGFAGVVR 360
EISFGTTKDK MLVIEQCKNS RAVTIFIRGG NKMIIEEAKR SLHDALCVIR NLIRDNRVVY 420
GGGAAEISCA LAVSQEADKC PTLEQYAMRA FADALEVIPM ALSENSGMNP IQTMTEVRAR 480
QVKESNPALG IDCLHKGSND MQYQHVIETL IGKKQQISLA TQMVRMILKI DDIRKPGESE 540
E 541 
Gene Ontology
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0009615; P:response to virus; IEA:Compara. 
Interpro
 IPR012718; Chap_CCT_epsi.
 IPR017998; Chaperone_TCP-1.
 IPR002194; Chaperonin_TCP-1_CS.
 IPR002423; Cpn60/TCP-1.
 IPR027409; GroEL-like_apical_dom.
 IPR027413; GROEL-like_equatorial.
 IPR027410; TCP-1-like_intermed. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
 PS00750; TCP1_1
 PS00751; TCP1_2
 PS00995; TCP1_3 
PRINTS
 PR00304; TCOMPLEXTCP1.